25 No. 2
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Prausnitz Awarded the 2002 Rossini Lecture
M. Prausnitz, a professor in the Chemical Engineering Department
of the University of California, Berkeley, and a faculty senior
scientist at the Lawrence Berkeley National Laboratory, was
awarded IUPACs 2002 Rossini Lecture, the highest international
award in the field of chemical thermodynamics.
presented the Rossini Lecture at the 17th IUPAC Conference
on Chemical Thermodynamics in Rostock, Germany on 28 July
2002. An abstract of his presentation on "Molecular Thermodynamics
for Some Applications in Biotechnology" appears
research is aimed at obtaining, interpreting, and correlating
thermodynamic properties of a variety of mixtures as required
for process and product design in the chemical and related
industries, including biotechnology. Toward that end, his
laboratory obtains experimental data, performs Monte-Carlo
molecular simulations, and develops molecular-thermodynamic
models based on the statistical mechanics of fluids and solids.
received his Ph.D. from Princeton in 1955. He is a member
of the National Academy of Sciences (1973), the National Academy
of Engineering (1979), and the American Academy of Arts and
Sciences (1988). He has received several honorary degrees:
Doctor of Engineering from the University of L Aquila,
Italy, in 1983, and the Technical University of Berlin, Germany,
in 1989, and a Doctor of Science from Princeton in 1995.
Thermodynamics for Some Applications in Biotechnology
Prausnitzs abstract presented at the 17th ICCT.
biotechnology sweeps the world, it is appropriate to remember
that the great virtue of thermodynamics is its broad range
of applicability. As a result, there is a growing literature
describing how chemical thermodynamics can be used to inform
processes for old and new biochemical products for industry
and medicine. A particular application of molecular thermodynamics
concerns separation of aqueous proteins by selective precipitation.
For this purpose, we need phase diagrams; for constructing
such diagrams, we need to understand not only the qualitative
nature of phase equilibria of aqueous proteins but also the
quantitative intermolecular forces between proteins in solution.
examples are given to show how aqueous protein-protein forces
can be calculated or measured to yield a potential of mean
force and how that potential is then used along with a statistical
thermodynamic model to establish liquid-liquid and liquid-crystal
equilibria. Such equilibria are useful not only for separation
processes but also for understanding diseases like Alzheimers,
cataracts, and sickle-cell anemia that appear to be caused
by protein agglomeration.
The Rossini Lecture - A brief
last modified 6 March 2003.
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